TWST1_HUMAN
ID TWST1_HUMAN Reviewed; 202 AA.
AC Q15672; A4D128; Q92487; Q99804;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Twist-related protein 1;
DE AltName: Full=Class A basic helix-loop-helix protein 38;
DE Short=bHLHa38;
DE AltName: Full=H-twist;
GN Name=TWIST1; Synonyms=BHLHA38, TWIST;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lung;
RX PubMed=9073070; DOI=10.1016/s0378-1119(96)00727-5;
RA Wang S.M., Coljee V.W., Pignolo R.J., Rotenberg M.O., Cristofalo V.J.,
RA Sierra F.;
RT "Cloning of the human twist gene: its expression is retained in adult
RT mesodermally-derived tissues.";
RL Gene 187:83-92(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Placenta;
RX PubMed=8995765; DOI=10.1007/s003359900269;
RA Bourgeois P., Stoetzel C., Bolcato-Bellemin A.-L., Mattei M.-G.,
RA Perrin-Schmitt F.;
RT "The human H-twist gene is located at 7p21 and encodes a B-HLH protein that
RT is 96% similar to its murine M-twist counterpart.";
RL Mamm. Genome 7:915-917(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SCS PRO-119;
RP ALA-ALA-LEU-ARG-LYS-ILE-ILE-135 INS AND LYS-ILE-ILE-PRO-THR-LEU-PRO-139
RP INS.
RX PubMed=8988166; DOI=10.1038/ng0197-36;
RA Howard T.D., Paznekas W.A., Green E.D., Chiang L.C., Ma N.,
RA Ortiz de Luna R.I., Delgado C.G., Gonzalez-Ramos M., Kline A.D., Jabs E.W.;
RT "Mutations in TWIST, a basic helix-loop-helix transcription factor, in
RT Saethre-Chotzen syndrome.";
RL Nat. Genet. 15:36-41(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9215678; DOI=10.1093/hmg/6.7.1079;
RA Krebs I., Weis I., Hudler M., Rommens J.M., Roth H., Scherer S.W.,
RA Tsui L.-C., Fuchtbauer E.-M., Grzeschik K.-H., Tsuji K., Kunz J.;
RT "Translocation breakpoint maps 5 kb 3-prime from TWIST in a patient
RT affected with Saethre-Chotzen syndrome.";
RL Hum. Mol. Genet. 6:1079-1086(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION.
RX PubMed=12553906; DOI=10.1016/s0092-8674(03)00002-3;
RA Sosic D., Richardson J.A., Yu K., Ornitz D.M., Olson E.N.;
RT "Twist regulates cytokine gene expression through a negative feedback loop
RT that represses NF-kappaB activity.";
RL Cell 112:169-180(2003).
RN [9]
RP VARIANTS SCS PRO-131 AND LYS-ILE-ILE-PRO-THR-LEU-PRO-139 INS.
RX PubMed=8988167; DOI=10.1038/ng0197-42;
RA el Ghouzzi V., le Merrer M., Perrin-Schmitt F., Lajeunie E., Benit P.,
RA Renier D., Bourgeois P., Bolcato-Bellemin A.-L., Munnich A.,
RA Bonaventure J.;
RT "Mutations of the TWIST gene in the Saethre-Chotzen syndrome.";
RL Nat. Genet. 15:42-46(1997).
RN [10]
RP INVOLVEMENT IN RSS.
RX PubMed=10465122;
RA Kunz J., Hudler M., Fritz B.;
RT "Identification of a frameshift mutation in the gene TWIST in a family
RT affected with Robinow-Sorauf syndrome.";
RL J. Med. Genet. 36:650-652(1999).
RN [11]
RP VARIANT SCS VAL-156.
RX PubMed=11754069; DOI=10.1002/ajmg.10065;
RA Seto M.L., Lee S.J., Sze R.W., Cunningham M.L.;
RT "Another TWIST on Baller-Gerold syndrome.";
RL Am. J. Med. Genet. 104:323-330(2001).
RN [12]
RP VARIANTS CRS1 THR-186 AND LEU-188.
RX PubMed=17343269; DOI=10.1002/ajmg.a.31630;
RA Seto M.L., Hing A.V., Chang J., Hu M., Kapp-Simon K.A., Patel P.K.,
RA Burton B.K., Kane A.A., Smyth M.D., Hopper R., Ellenbogen R.G.,
RA Stevenson K., Speltz M.L., Cunningham M.L.;
RT "Isolated sagittal and coronal craniosynostosis associated with TWIST box
RT mutations.";
RL Am. J. Med. Genet. A 143:678-686(2007).
RN [13]
RP VARIANTS SER-83 AND GLY-95, FUNCTION, AND CHARACTERIZATION OF VARIANTS
RP SER-83 AND GLY-95.
RX PubMed=25981568; DOI=10.1007/s00246-015-1202-9;
RA Deng X., Pan H., Wang J., Wang B., Cheng Z., Cheng L., Zhao L., Li H.,
RA Ma X.;
RT "Functional analysis of two novel mutations in TWIST1 protein motifs found
RT in ventricular septal defect patients.";
RL Pediatr. Cardiol. 36:1602-1609(2015).
RN [14]
RP INVOLVEMENT IN SWCOS, AND VARIANTS SWCOS GLY-117 AND VAL-117.
RX PubMed=28369379; DOI=10.1093/hmg/ddx107;
RA Kim S., Twigg S.R.F., Scanlon V.A., Chandra A., Hansen T.J., Alsubait A.,
RA Fenwick A.L., McGowan S.J., Lord H., Lester T., Sweeney E., Weber A.,
RA Cox H., Wilkie A.O.M., Golden A., Corsi A.K.;
RT "Localized TWIST1 and TWIST2 basic domain substitutions cause four distinct
RT human diseases that can be modeled in Caenorhabditis elegans.";
RL Hum. Mol. Genet. 26:2118-2132(2017).
CC -!- FUNCTION: Acts as a transcriptional regulator. Inhibits myogenesis by
CC sequestrating E proteins, inhibiting trans-activation by MEF2, and
CC inhibiting DNA-binding by MYOD1 through physical interaction. This
CC interaction probably involves the basic domains of both proteins. Also
CC represses expression of pro-inflammatory cytokines such as TNFA and
CC IL1B. Regulates cranial suture patterning and fusion. Activates
CC transcription as a heterodimer with E proteins. Regulates gene
CC expression differentially, depending on dimer composition. Homodimers
CC induce expression of FGFR2 and POSTN while heterodimers repress FGFR2
CC and POSTN expression and induce THBS1 expression. Heterodimerization is
CC also required for osteoblast differentiation. Represses the activity of
CC the circadian transcriptional activator: NPAS2-ARNTL/BMAL1 heterodimer
CC (By similarity). {ECO:0000250|UniProtKB:P26687,
CC ECO:0000269|PubMed:12553906, ECO:0000269|PubMed:25981568}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Homodimer or heterodimer with E proteins such as TCF3. ID1
CC binds preferentially to TCF3 but does not interact efficiently with
CC TWIST1 so ID1 levels control the amount of TCF3 available to dimerize
CC with TWIST1 and thus determine the type of dimer formed (By
CC similarity). {ECO:0000250|UniProtKB:P26687}.
CC -!- INTERACTION:
CC Q15672; O60885: BRD4; NbExp=7; IntAct=EBI-1797287, EBI-723869;
CC Q15672; O60885-1: BRD4; NbExp=9; IntAct=EBI-1797287, EBI-9345088;
CC Q15672; P15036: ETS2; NbExp=2; IntAct=EBI-1797287, EBI-1646991;
CC Q15672; Q9UN86: G3BP2; NbExp=2; IntAct=EBI-1797287, EBI-1044298;
CC Q15672; P42858: HTT; NbExp=3; IntAct=EBI-1797287, EBI-466029;
CC Q15672; Q92831: KAT2B; NbExp=2; IntAct=EBI-1797287, EBI-477430;
CC Q15672; Q92993: KAT5; NbExp=2; IntAct=EBI-1797287, EBI-399080;
CC Q15672; Q9NQR1: KMT5A; NbExp=5; IntAct=EBI-1797287, EBI-1268946;
CC Q15672; P15923-1: TCF3; NbExp=6; IntAct=EBI-1797287, EBI-769645;
CC Q15672; P15884: TCF4; NbExp=8; IntAct=EBI-1797287, EBI-533224;
CC Q15672; P04637: TP53; NbExp=10; IntAct=EBI-1797287, EBI-366083;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Subset of mesodermal cells.
CC -!- DISEASE: Saethre-Chotzen syndrome (SCS) [MIM:101400]: A
CC craniosynostosis syndrome characterized by coronal synostosis,
CC brachycephaly, low frontal hairline, facial asymmetry, hypertelorism,
CC broad halluces, and clinodactyly. {ECO:0000269|PubMed:11754069,
CC ECO:0000269|PubMed:8988166, ECO:0000269|PubMed:8988167}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Robinow-Sorauf syndrome (RSS) [MIM:180750]: An autosomal
CC dominant syndrome characterized by craniosynostosis, asymmetry of
CC orbits, flat face, hypertelorism, a thin, long, and pointed nose,
CC shallow orbits, strabismus, and broad great toes with a duplication of
CC the distal phalanx. RSS is clinically similar to Saethre-Chotzen
CC syndrome, with the most characteristic additional feature in Robinow-
CC Sorauf syndrome being a bifid or partially duplicated hallux.
CC {ECO:0000269|PubMed:10465122}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Craniosynostosis 1 (CRS1) [MIM:123100]: A primary abnormality
CC of skull growth involving premature fusion of one or more cranial
CC sutures. The growth velocity of the skull often cannot match that of
CC the developing brain resulting in an abnormal head shape and, in some
CC cases, increased intracranial pressure, which must be treated promptly
CC to avoid permanent neurodevelopmental disability.
CC {ECO:0000269|PubMed:17343269}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Sweeney-Cox syndrome (SWCOS) [MIM:617746]: An autosomal
CC dominant syndrome characterized by facial dysostosis, including
CC hypertelorism, deficiencies of the eyelids and facial bones, cleft
CC palate/velopharyngeal insufficiency, and low-set cupped ears.
CC {ECO:0000269|PubMed:28369379}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TWIST1ID44296ch7p21.html";
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DR EMBL; X91662; CAA62850.1; -; Genomic_DNA.
DR EMBL; X99268; CAA67664.1; -; mRNA.
DR EMBL; U80998; AAC50930.1; -; Genomic_DNA.
DR EMBL; Y10871; CAA71821.1; -; Genomic_DNA.
DR EMBL; AC003986; AAC60381.2; -; Genomic_DNA.
DR EMBL; CH236948; EAL24279.1; -; Genomic_DNA.
DR EMBL; BC036704; AAH36704.1; -; mRNA.
DR CCDS; CCDS5367.1; -.
DR PIR; G01204; G01204.
DR RefSeq; NP_000465.1; NM_000474.3.
DR RefSeq; XP_011513798.1; XM_011515496.1.
DR PDB; 2MJV; NMR; -; A=68-79.
DR PDBsum; 2MJV; -.
DR AlphaFoldDB; Q15672; -.
DR SMR; Q15672; -.
DR BioGRID; 113142; 57.
DR CORUM; Q15672; -.
DR DIP; DIP-45974N; -.
DR IntAct; Q15672; 32.
DR MINT; Q15672; -.
DR STRING; 9606.ENSP00000242261; -.
DR iPTMnet; Q15672; -.
DR PhosphoSitePlus; Q15672; -.
DR BioMuta; TWIST1; -.
DR DMDM; 2498009; -.
DR MassIVE; Q15672; -.
DR PaxDb; Q15672; -.
DR PeptideAtlas; Q15672; -.
DR PRIDE; Q15672; -.
DR ProteomicsDB; 60700; -.
DR ABCD; Q15672; 7 sequenced antibodies.
DR Antibodypedia; 11900; 649 antibodies from 39 providers.
DR DNASU; 7291; -.
DR Ensembl; ENST00000242261.6; ENSP00000242261.5; ENSG00000122691.13.
DR GeneID; 7291; -.
DR KEGG; hsa:7291; -.
DR MANE-Select; ENST00000242261.6; ENSP00000242261.5; NM_000474.4; NP_000465.1.
DR UCSC; uc003sum.3; human.
DR CTD; 7291; -.
DR DisGeNET; 7291; -.
DR GeneCards; TWIST1; -.
DR GeneReviews; TWIST1; -.
DR HGNC; HGNC:12428; TWIST1.
DR HPA; ENSG00000122691; Tissue enhanced (adipose tissue, breast).
DR MalaCards; TWIST1; -.
DR MIM; 101400; phenotype.
DR MIM; 123100; phenotype.
DR MIM; 180750; phenotype.
DR MIM; 601622; gene.
DR MIM; 617746; phenotype.
DR neXtProt; NX_Q15672; -.
DR OpenTargets; ENSG00000122691; -.
DR Orphanet; 35099; Non-syndromic bicoronal craniosynostosis.
DR Orphanet; 35093; Non-syndromic sagittal craniosynostosis.
DR Orphanet; 794; Saethre-Chotzen syndrome.
DR PharmGKB; PA37088; -.
DR VEuPathDB; HostDB:ENSG00000122691; -.
DR eggNOG; KOG4447; Eukaryota.
DR GeneTree; ENSGT00940000162831; -.
DR HOGENOM; CLU_112073_0_0_1; -.
DR InParanoid; Q15672; -.
DR OMA; XSSSAGI; -.
DR OrthoDB; 1595261at2759; -.
DR PhylomeDB; Q15672; -.
DR TreeFam; TF315153; -.
DR PathwayCommons; Q15672; -.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-8878166; Transcriptional regulation by RUNX2.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR SignaLink; Q15672; -.
DR SIGNOR; Q15672; -.
DR BioGRID-ORCS; 7291; 16 hits in 1096 CRISPR screens.
DR ChiTaRS; TWIST1; human.
DR GeneWiki; Twist_transcription_factor; -.
DR GenomeRNAi; 7291; -.
DR Pharos; Q15672; Tbio.
DR PRO; PR:Q15672; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q15672; protein.
DR Bgee; ENSG00000122691; Expressed in periodontal ligament and 161 other tissues.
DR ExpressionAtlas; Q15672; baseline and differential.
DR Genevisible; Q15672; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043425; F:bHLH transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0070888; F:E-box binding; IDA:BHF-UCL.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0001221; F:transcription coregulator binding; IEA:Ensembl.
DR GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL.
DR GO; GO:0003253; P:cardiac neural crest cell migration involved in outflow tract morphogenesis; IEA:Ensembl.
DR GO; GO:2000793; P:cell proliferation involved in heart valve development; IMP:BHF-UCL.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IMP:BHF-UCL.
DR GO; GO:0060363; P:cranial suture morphogenesis; TAS:BHF-UCL.
DR GO; GO:0032502; P:developmental process; IBA:GO_Central.
DR GO; GO:0060900; P:embryonic camera-type eye formation; IMP:BHF-UCL.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:BHF-UCL.
DR GO; GO:0042733; P:embryonic digit morphogenesis; TAS:BHF-UCL.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IEA:Ensembl.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl.
DR GO; GO:0003203; P:endocardial cushion morphogenesis; IEA:Ensembl.
DR GO; GO:0061029; P:eyelid development in camera-type eye; IMP:BHF-UCL.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0003183; P:mitral valve morphogenesis; IEA:Ensembl.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:2000773; P:negative regulation of cellular senescence; IMP:BHF-UCL.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IMP:BHF-UCL.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IEA:Ensembl.
DR GO; GO:2000780; P:negative regulation of double-strand break repair; IMP:BHF-UCL.
DR GO; GO:0035067; P:negative regulation of histone acetylation; IEA:Ensembl.
DR GO; GO:0033128; P:negative regulation of histone phosphorylation; IMP:BHF-UCL.
DR GO; GO:0010936; P:negative regulation of macrophage cytokine production; IEA:Ensembl.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:BHF-UCL.
DR GO; GO:2000276; P:negative regulation of oxidative phosphorylation uncoupler activity; IEA:Ensembl.
DR GO; GO:0035359; P:negative regulation of peroxisome proliferator activated receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IMP:BHF-UCL.
DR GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; IEA:Ensembl.
DR GO; GO:0045843; P:negative regulation of striated muscle tissue development; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0001764; P:neuron migration; IEA:Ensembl.
DR GO; GO:0042476; P:odontogenesis; IEA:Ensembl.
DR GO; GO:0001503; P:ossification; TAS:BHF-UCL.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0042473; P:outer ear morphogenesis; TAS:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; NAS:BHF-UCL.
DR GO; GO:2000147; P:positive regulation of cell motility; IMP:BHF-UCL.
DR GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IDA:CACAO.
DR GO; GO:2000802; P:positive regulation of endocardial cushion to mesenchymal transition involved in heart valve formation; IEA:Ensembl.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
DR GO; GO:0032000; P:positive regulation of fatty acid beta-oxidation; IMP:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:BHF-UCL.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:BHF-UCL.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IMP:BHF-UCL.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:BHF-UCL.
DR GO; GO:0030500; P:regulation of bone mineralization; IMP:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR Gene3D; 4.10.280.10; -; 1.
DR IDEAL; IID00624; -.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR015789; Twist-related.
DR PANTHER; PTHR23349:SF64; PTHR23349:SF64; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Biological rhythms; Craniosynostosis;
KW Developmental protein; Differentiation; Disease variant; DNA-binding;
KW Myogenesis; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..202
FT /note="Twist-related protein 1"
FT /id="PRO_0000127483"
FT DOMAIN 108..159
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..191
FT /note="Sufficient for transactivation activity"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 83
FT /note="G -> S (found in a patient with non-syndromic
FT ventricular septal defect; unknown pathological
FT significance; loss of function in negative regulation of
FT transcription from E-cadherin promoter; dbSNP:rs545987863)"
FT /evidence="ECO:0000269|PubMed:25981568"
FT /id="VAR_077470"
FT VARIANT 95
FT /note="S -> G (no effect on negative regulation of
FT transcription from E-cadherin promoter; dbSNP:rs575299986)"
FT /evidence="ECO:0000269|PubMed:25981568"
FT /id="VAR_077471"
FT VARIANT 117
FT /note="E -> G (in SWCOS; dbSNP:rs1554442016)"
FT /evidence="ECO:0000269|PubMed:28369379"
FT /id="VAR_080515"
FT VARIANT 117
FT /note="E -> V (in SWCOS; dbSNP:rs1554442016)"
FT /evidence="ECO:0000269|PubMed:28369379"
FT /id="VAR_080516"
FT VARIANT 119
FT /note="Q -> P (in SCS; dbSNP:rs104894057)"
FT /evidence="ECO:0000269|PubMed:8988166"
FT /id="VAR_004495"
FT VARIANT 131
FT /note="L -> P (in SCS; dbSNP:rs121909189)"
FT /evidence="ECO:0000269|PubMed:8988167"
FT /id="VAR_004496"
FT VARIANT 135
FT /note="I -> IAALRKII (in SCS)"
FT /id="VAR_004497"
FT VARIANT 139
FT /note="P -> PKIIPTLP (in SCS)"
FT /id="VAR_004498"
FT VARIANT 156
FT /note="I -> V (in SCS; variant form with features
FT overlapping Baller-Gerold syndrome; dbSNP:rs104894059)"
FT /evidence="ECO:0000269|PubMed:11754069"
FT /id="VAR_015219"
FT VARIANT 186
FT /note="A -> T (in CRS1; dbSNP:rs121909190)"
FT /evidence="ECO:0000269|PubMed:17343269"
FT /id="VAR_034985"
FT VARIANT 188
FT /note="S -> L (in CRS1; dbSNP:rs121909191)"
FT /evidence="ECO:0000269|PubMed:17343269"
FT /id="VAR_034986"
FT CONFLICT 32
FT /note="G -> A (in Ref. 2; CAA67664)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="G -> A (in Ref. 2; CAA67664)"
FT /evidence="ECO:0000305"
FT CONFLICT 41
FT /note="S -> T (in Ref. 1; CAA62850 and 4; CAA71821)"
FT /evidence="ECO:0000305"
FT CONFLICT 45
FT /note="S -> T (in Ref. 1; CAA62850 and 4; CAA71821)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="Missing (in Ref. 1; CAA62850 and 4; CAA71821)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="G -> A (in Ref. 2; CAA67664)"
FT /evidence="ECO:0000305"
FT CONFLICT 92
FT /note="G -> GGGGG (in Ref. 2; CAA67664)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 202 AA; 20954 MW; 9394E4351BA1D081 CRC64;
MMQDVSSSPV SPADDSLSNS EEEPDRQQPP SGKRGGRKRR SSRRSAGGGA GPGGAAGGGV
GGGDEPGSPA QGKRGKKSAG CGGGGGAGGG GGSSSGGGSP QSYEELQTQR VMANVRERQR
TQSLNEAFAA LRKIIPTLPS DKLSKIQTLK LAARYIDFLY QVLQSDELDS KMASCSYVAH
ERLSYAFSVW RMEGAWSMSA SH
